Main profile

Pankaj Vidyadhar Alone

School: 

Biological Sciences

Designation: 

Reader-F

Education: 

1996-2001 : Ph.D. (Molecular Biology) National Institute of Immunology, J.N.U. Campus New Delhi 110 067, INDIA 

Thesis Title : Structure-Function Studies of Engineered N-terminal α1 Helix of Heat Labile Enterotoxin Chain B in Escherichia coli and Vibrio cholerae

1994-1996 : M. Sc. (Biochemistry) 

Department of Biochemistry, Nagpur University, Nagpur, Maharashtra, INDIA

1991-1994 : B. Sc. (Microbiology, Biochemistry, Chemistry) 

Nagpur University, Nagpur, Maharashtra, INDIA

Specialisation: 

Molecular Genetic Study of Protein Biosynthesis

Awards: 

NIH Fellows Award for Research Excellence (NIH-FARE) for years 2005 and 2006.

Publications: 

• Antony A C, Ram AK, Dutta K and Alone PV. Ribosomal mutation in helix 32 of 18S rRNA alters fidelity of eukaryotic translation start site selection. (2019) FEBS Lett.
• Antony A C and Alone PV. Fidelity of HIS4 start codon selection influences 3-amino-1,2,4-triazole sensitivity in GTPase activating protein function defective eIF5. (2018) J Genet. 97 (4): 953-964.
• Antony A C and Alone PV. Defect in the GTPase activating protein (GAP) function of eIF5 causes repression of GCN4 translation. (2017) Biochem Biophys Res Commun. 486 (4):1110-1115.
• Alone PV, Cao C and Dever TE. Translation initiation factor eIF2γ mutants alter start codon selection independent of Met-tRNA_i^Met binding. (2008) Mol Cell Biol. 28 (22): 6877-88.
• Alone PV and Garg LC. Secretory and GM₁ receptor binding role of N-Terminal end of LTB in Vibrio Cholerae. (2008) Biochem Biophy Res Comm. 376 (4): 770-4.
• Alone PV, Malik G, Krishnan A and Garg LC. Deletion mutations in N-terminal α1 helix render heat labile enterotoxin B subunit susceptible to degradation. (2007) Proc Natl Acad Sci (USA). 104 (41): 16056-61
• Alone PV and Dever TE. Direct binding of translation initiation factor eIF2γ-G domain to its GTPase-activating and GDP-GTP exchange factors eIF5 and eIF2Bε. (2006) J Biol Chem. 281(18):12636-44.
• Roll-Mecak A, Alone P, Cao C, Dever TE and Burley SK. X-ray structure of translation initiation factor eIF2γ: implications for tRNA and eIF2α binding, (2004) J Biol Chem. 279 (11):10634-42.

Research: 

The fundamental difference between prokaryotic and eukaryotic translation initiation is that the former uses Shine-Dalgarno (SD) sequence on the mRNA to recruit small ribosome subunit and locate AUG codon or rarely GUC, CUC or UUG codon as a translation start site, while the latter uses eIF4F complex to bind mRNA and locate AUG codon or rarely CUG, UUG or GUC as a start codon by 5` to 3` scanning mechanism. Some of the examples listed below shows the involvement of non-AUG codon as a translation start signal.

In Saccharomyces cerevisiae, GRS1 encodes two isoforms of Glycyl-tRNA synthetases, one initiates from upstream in-frame UUG codon (encoding signal sequence for mitochondrial import) while the regular cytoplasmic version initiates from downstream AUG codon. For the synthesis of Alanine t-RNA synthetase (ALA1) protein a consecutive ACG ACG codon are utilized as an alternate translation start site. It has been reported recently that MHC class-I molecule can load antigenic precursor which is synthesized by using CUG as an initiation codon recognized by leucine tRNA and non-conventional eIF2A translation initiation factor. A genome wide ribosomal profiling analysis of vivo translation study reported that translation initiation from upstream non-AUG codon is widespread in S. cerevisiae under starvation condition. However, the importance and the basic mechanism for these initiations are still unclear. A number of yeast mutants have been identified that are able to initiate at the non-AUG codons. These mutants were designated as Sui^— (Suppressor of initiation) phenotypes. Sui^— phenotypes are novel mutations that causes break down of AUG codon selection fidelity. Thus, Sui^— mutants provide an important tool to understand the molecular mechanism of non-AUG codon selection.

The focus of our lab is to understand the molecular mechanism of non-canonical translation initiation processes in Saccharomyces cerevisiae using molecular genetic techniques.

The key questions are as follows:

• How Sui^— mutants recognize UUG codon as a start codon?
• Does 18S rRNA residues play critical role in UUG codon recognition by Sui^— mutant?
• Does cis-acting elements on mRNA plays critical role in non-AUG codon recognition by Sui^— mutants?
• Are there special trans-acting factors involved in non-AUG codon selection?

 

Teaching: 

• Molecular Biology (B304) for MSc students
• Molecular Biology Laboratory (B343) for MSc students
• Advance Molecular Biology (B551/B701) for MSc and Ph.D students 

Contacts: 

Pankaj V. Alone

National Institute of Science Education and Research

Jatni-Khurda Road

District- Khurda, PIN- 752050, Odisha, India
Phones : +91-674-249-4205

pankaj@niser.ac.in

Phone No.: 

+91-674-249-4205

Room No.: 

205

Personal Page: 

http://www.niser.ac.in/~pankaj

Group Members: 

Anup Kumar, Aranyadip,  Kalloly, Amiyaranjan , Ankita Priyadarshini, Neha 

 

Other Links: 

http://www.yeastgenome.org/

http://apollo.chemistry.gatech.edu/RiboVision/